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PMID: 2306129 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Chlorophyll-free chromoplasts from daffodil contain most of the enzymes for chlorophyll synthesis in a highly active form.

Archives of biochemistry and biophysics ·Vol. 277 ·No. 1 ·1990-02-15 ·Pages 94-100

Lützow M, Kleinig H

Abstract

Chromoplasts isolated from chlorophyll-free daffodil flowers utilize in vitro delta-aminolevulinic acid (ALA) as precursor for the synthesis of large amounts of at least nine different products. Their identification as intermediates of the chlorophyll biosynthetic pathway demonstrates the presence of the majority of the respective enzymes in this nongreen plastid preparation. Porphobilinogen synthase was investigated more closely and found to be similar in its properties to the corresponding enzyme from other plastid sources. Protoporphyrin IX was also accepted as a substrate by chromoplast homogenate; here, as in the case of ALA as a substrate, Mg-protoporphyrin IX monomethyl ester was the last product formed. Formation of the isocyclic chlorophyll ring was not observed.

MeSH Terms
Aminolevulinic Acid/metabolism Chlorophyll/biosynthesis Chloroplasts/enzymology Chromatography, High Pressure Liquid Chromatography, Thin Layer Kinetics Plants/enzymology Porphobilinogen Synthase/metabolism Porphyrins/isolation & purification
Chemicals
Porphyrins Chlorophyll Aminolevulinic Acid Porphobilinogen Synthase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Lützow M
Institut für Biologie II, Universität Freiburg, Federal Republic of Germany.
Kleinig H
Article Info
Journal
Archives of biochemistry and biophysics
Abbr.
Arch Biochem Biophys
ISSN
0003-9861
Published
1990-02-15
Pages
94-100
Language
English
Region
United States
NLM ID
0372430
Subset
IM
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